Key result
CVB3 nonstructural protein 2A upregulates and activates SREBP1a, and inhibition of SREBP1 decreases CVB3 virus replication, revealing a potential novel therapeutic target.
CVB3 nonstructural protein 2A upregulates SREBP1a to promote lipid accumulation and viral replication, identifying SREBP1 as a potential therapeutic target for viral myocarditis.
Coxsackievirus B3 (CVB3) infection is the leading cause of viral myocarditis, but effective vaccines and antiviral therapies against CVB3 infection are still lacking. It is important to understand the precise interactions between host and virus for the rational design of effective therapies. During infection, CVB3 disrupts and exploits host lipid metabolism to promote excessive lipid accumulation, which benefits virus replication. SREBP1 is the master regulator of cellular lipid metabolism. Here, we report that one of the viral nonstructural proteins, 2A, upregulates and activates SREBP1a. Furthermore, we find that inhibition of SREBP1 decreases CVB3 virus replication. These results reveal the regulation of SREBP1a expression by 2A and the roles of SREBP1 in lipid accumulation and viral replication during CVB3 infection. Our findings provide a new insight into CVB3 host interactions and inform a potential novel therapeutic target for this important pathogen.
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Wang et al. (2018) studied Coxsackievirus B3 (CVB3) infection / viral myocarditis. SREBP1 inhibition was evaluated on CVB3 virus replication and SREBP1a activation. CVB3 nonstructural protein 2A upregulates and activates SREBP1a, and inhibition of SREBP1 decreases CVB3 virus replication, revealing a potential novel therapeutic target.
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